Research workbench
NMR study of the SH3 domain from fyn proto-oncogene tyrosine kinase kinase complexed with the synthetic peptide P2L corresponding to residues 91-104 of the P85 subunit of PI3-kinase, minimized average (probmap) structure
Analyse NMR study of the SH3 domain from fyn proto-oncogene tyrosine kinase kinase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1AZG
- Type
- protein
- Length
- 72 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P27986, P06241
Structure
solution nmr · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 14 | — | P27986 |
| B | — | protein | 58 | — | P06241 |
Compared structures
- 1AZG · NMR study of the SH3 domain from fyn proto-oncogene tyrosine kinase kinase complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
- P06241 · AlphaFold monomer V2.0 prediction for tyrosine-protein kinase fyn (P06241) · a predicted model of the same protein · chain B against A, TM-score 0.91
- P27986 · AlphaFold monomer V2.0 prediction for phosphatidylinositol 3-kinase regulatory subunit… · a predicted model of the same protein · chain A against A, TM-score 0.23
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P27986
- Every structure of UniProt P06241
- Elsewhere: RCSB PDB 1AZG · PDBe 1AZG · UniProt P27986 · UniProt P06241
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